Lance M. Hellman
University of Notre Dame
37 Papers
87 Citations
Lance M. Hellman is an academic researcher from University of Notre Dame. The author has contributed to research in topics: T-cell receptor & Major histocompatibility complex. The author has an hindex of 20, co-authored 35 publications. Previous affiliations of Lance M. Hellman include University of Kentucky & University of Massachusetts Amherst.
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Papers
Electrophoretic mobility shift assay (EMSA) for detecting protein-nucleic acid interactions.
Lance M. Hellman,Michael Fried +1 more
TL;DR: The most important factors that determine the stabilities and electrophoretic mobilities of complexes under assay conditions are identified and commonly used variants are discussed.
Cutting Edge: Evidence for a Dynamically Driven T Cell Signaling Mechanism
William F. Hawse,Matthew M. Champion,Michelle V. Joyce,Lance M. Hellman,Moushumi Hossain,Veronica Ryan,Brian G. Pierce,Zhiping Weng,Brian M. Baker +8 more
TL;DR: Ligation globally rigidifies the TCR, which via entropic and packing effects will promote associations with neighboring proteins and enhance the stability of existing complexes, raising the possibility that TCR triggering could involve a dynamically driven, allosteric mechanism.
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Furin Processing of Semaphorin 3F Determines Its Anti-Angiogenic Activity by Regulating Direct Binding and Competition for Neuropilin
TL;DR: This work demonstrates that furin activation of the C-terminus of Sema3F produces a species that potently inhibits the binding of VEGF to neuropilin, and provides a mechanistic basis for understanding the anti-angiogenic activity of semaphorin as well as the physical interaction and competition between neuro pilin ligands.
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Dynamically Driven Allostery in MHC Proteins: Peptide-Dependent Tuning of Class I MHC Global Flexibility.
Cory M. Ayres,Esam T. Abualrous,Alistair Bailey,Christian Abraham,Lance M. Hellman,Steven A. Corcelli,Frank Noé,Tim Elliott,Brian M. Baker +8 more
TL;DR: The results demonstrate that the class I MHC protein is a highly tunable peptide sensor whose physical properties vary considerably with bound peptide and suggest a role for dynamically driven allostery in the immunological function of MHC proteins.
FOXO3–NF-κB RelA Protein Complexes Reduce Proinflammatory Cell Signaling and Function
Matthew G. Thompson,Michelle Larson,Amy Vidrine,Kelly Barrios,Flor Navarro,Kaitlyn Meyers,Patricia E. Simms,Kushal Prajapati,Lennox Chitsike,Lance M. Hellman,Brian M. Baker,Stephanie K. Watkins +11 more
TL;DR: This study demonstrates a novel mechanism involving FOXO3 and NF-κB RelA that controls myeloid cell signaling and impacts their immune-suppressive nature and identifies for the first time, to the knowledge, a direct protein–protein interaction in tumor-associated DCs.
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